LSRG_YERPB
ID LSRG_YERPB Reviewed; 96 AA.
AC B2K3F6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
DE EC=5.3.1.32 {ECO:0000255|HAMAP-Rule:MF_02051};
DE AltName: Full=Autoinducer 2-degrading protein LsrG {ECO:0000255|HAMAP-Rule:MF_02051};
DE Short=AI-2-degrading protein LsrG {ECO:0000255|HAMAP-Rule:MF_02051};
DE AltName: Full=Phospho-(S)-4,5-dihydroxy-2,3-pentanedione isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
DE AltName: Full=Phospho-AI-2 isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
GN Name=lsrG {ECO:0000255|HAMAP-Rule:MF_02051}; OrderedLocusNames=YPTS_0571;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the degradation of phospho-AI-2, thereby
CC terminating induction of the lsr operon and closing the AI-2 signaling
CC cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-
CC phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-
CC phosphonooxypentane-2,4-dione (P-HPD). {ECO:0000255|HAMAP-
CC Rule:MF_02051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxy-3,4-dioxopentyl phosphate = 3-hydroxy-2,4-
CC dioxopentyl phosphate; Xref=Rhea:RHEA:44360, ChEBI:CHEBI:71677,
CC ChEBI:CHEBI:84359; EC=5.3.1.32; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02051};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02051}.
CC -!- SIMILARITY: Belongs to the LsrG family. {ECO:0000255|HAMAP-
CC Rule:MF_02051}.
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DR EMBL; CP001048; ACC87555.1; -; Genomic_DNA.
DR RefSeq; WP_002209186.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K3F6; -.
DR SMR; B2K3F6; -.
DR GeneID; 66843034; -.
DR KEGG; ypb:YPTS_0571; -.
DR PATRIC; fig|502801.10.peg.4247; -.
DR OMA; DTVAPMM; -.
DR BioCyc; YPSE502801:YPTS_RS02970-MON; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02051; LsrG; 1.
DR InterPro; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR033672; LsrG.
DR Pfam; PF03992; ABM; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS51725; ABM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase.
FT CHAIN 1..96
FT /note="(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione
FT isomerase"
FT /id="PRO_0000351583"
FT DOMAIN 2..91
FT /note="ABM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
SQ SEQUENCE 96 AA; 11098 MW; FB8E869AEC86AA21 CRC64;
MHVTLVEINV KEDKVDQFIE VFRANHLGSI REAGNLRFDV LRDEHIPTRF YIYEAYTDEA
AVAIHKTTPH YLQCVEQLAP LMTGPRKKTV FIGLMP